Mechanistic insights into the role of Hop2-Mnd1 in meiotic homologous DNA pairing
Copyright policy )Mechanistic insights into the role of Hop2-Mnd1 in meiotic homologous DNA pairing
The Hop2-Mnd1 complex functions with the DMC1 recombinase in meiotic recombination. Hop2-Mnd1 stabilizes the DMC1-single-stranded DNA (ssDNA) filament and promotes the capture of the double-stranded DNA partner by the recombinase filament to assemble the synaptic complex. Herein, we define the action mechanism of Hop2-Mnd1 in DMC1-mediated recombination. Small angle X-ray scattering analysis and electron microscopy reveal that the heterodimeric Hop2-Mnd1 is a V-shaped molecule. We show that the protein complex harbors three distinct DNA binding sites, and determine their functional relevance. Specifically, the N-terminal double-stranded DNA binding functions of Hop2 and Mnd1 co-operate to mediate synaptic complex assembly, whereas ssDNA binding by the Hop2 C-terminus helps stabilize the DMC1-ssDNA filament. A model of the Hop2-Mnd1-DMC1-ssDNA ensemble is proposed to explain how it mediates homologous DNA pairing in meiotic recombination.
- Oklahoma Medical Research Foundation United States
- School of Medicine Yale University United States
- Tsinghua University China (People's Republic of)
- National Institute of Health Pakistan
- National Institutes of Health United States
Binding Sites, Cell Cycle Proteins, DNA, Genome Integrity, Repair and Replication, Protein Structure, Tertiary, DNA-Binding Proteins, Recombinases, Meiosis, Mice, Animals, Point Mutation, Protein Multimerization, Homologous Recombination
Binding Sites, Cell Cycle Proteins, DNA, Genome Integrity, Repair and Replication, Protein Structure, Tertiary, DNA-Binding Proteins, Recombinases, Meiosis, Mice, Animals, Point Mutation, Protein Multimerization, Homologous Recombination
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